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Database: UniProt
Entry: A0A1I3AY12_9GAMM
LinkDB: A0A1I3AY12_9GAMM
Original site: A0A1I3AY12_9GAMM 
ID   A0A1I3AY12_9GAMM        Unreviewed;       206 AA.
AC   A0A1I3AY12;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Small ribosomal subunit protein uS4 {ECO:0000256|ARBA:ARBA00035254, ECO:0000256|HAMAP-Rule:MF_01306};
GN   Name=rpsD {ECO:0000256|HAMAP-Rule:MF_01306};
GN   ORFNames=SAMN04487959_105212 {ECO:0000313|EMBL:SFH54706.1};
OS   Halomonas xianhensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=442341 {ECO:0000313|EMBL:SFH54706.1, ECO:0000313|Proteomes:UP000199040};
RN   [1] {ECO:0000313|EMBL:SFH54706.1, ECO:0000313|Proteomes:UP000199040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.6848 {ECO:0000313|EMBL:SFH54706.1,
RC   ECO:0000313|Proteomes:UP000199040};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC       to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_01306}.
CC   -!- FUNCTION: With S5 and S12 plays an important role in translational
CC       accuracy. {ECO:0000256|HAMAP-Rule:MF_01306}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S5. The
CC       interaction surface between S4 and S5 is involved in control of
CC       translational fidelity. {ECO:0000256|HAMAP-Rule:MF_01306}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC       {ECO:0000256|ARBA:ARBA00007465, ECO:0000256|HAMAP-Rule:MF_01306,
CC       ECO:0000256|RuleBase:RU003699}.
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DR   EMBL; FOPY01000005; SFH54706.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I3AY12; -.
DR   STRING; 442341.SAMN04487959_105212; -.
DR   Proteomes; UP000199040; Unassembled WGS sequence.
DR   GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00165; S4; 1.
DR   Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR   HAMAP; MF_01306_B; Ribosomal_S4_B; 1.
DR   InterPro; IPR022801; Ribosomal_uS4.
DR   InterPro; IPR005709; Ribosomal_uS4_bac-type.
DR   InterPro; IPR018079; Ribosomal_uS4_CS.
DR   InterPro; IPR001912; Ribosomal_uS4_N.
DR   InterPro; IPR002942; S4_RNA-bd.
DR   InterPro; IPR036986; S4_RNA-bd_sf.
DR   NCBIfam; TIGR01017; rpsD_bact; 1.
DR   PANTHER; PTHR11831; 30S 40S RIBOSOMAL PROTEIN; 1.
DR   PANTHER; PTHR11831:SF4; 37S RIBOSOMAL PROTEIN NAM9, MITOCHONDRIAL; 1.
DR   Pfam; PF00163; Ribosomal_S4; 1.
DR   Pfam; PF01479; S4; 1.
DR   SMART; SM01390; Ribosomal_S4; 1.
DR   SMART; SM00363; S4; 1.
DR   SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR   PROSITE; PS00632; RIBOSOMAL_S4; 1.
DR   PROSITE; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000199040};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_01306};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_01306};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01306};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_01306}.
FT   DOMAIN          3..95
FT                   /note="Small ribosomal subunit protein uS4 N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01390"
FT   DOMAIN          96..160
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
SQ   SEQUENCE   206 AA;  23351 MW;  AC1EB1D11F49FBD8 CRC64;
     MARYIGPKCK LSRREGTDLF LKSGVTPFEK KCKSEQIPGV HGQRRQRLSD YGLQLREKQK
     VRRIYGVLEK QFRNYYKEAA RMKGATGELL LQLLESRLDN VVYRMGFGAT RAEARQLVSH
     KAITVNGRTV NVASYQVKPG DVVAVREKAK NQARIQHALQ LAGQRGDIAW IDVDSKKMEG
     TFKAVPERGD LSADINENLI VELYSK
//
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